P43815
Gene name |
alaS |
Protein name |
Alanine--tRNA ligase |
Names |
Alanyl-tRNA synthetase, AlaRS |
Species |
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
KEGG Pathway |
hin:HI_0814 |
EC number |
6.1.1.7: Ligases forming aminoacyl-tRNA and related compounds |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P43815
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P43815-F1 | Predicted | AlphaFoldDB |
No variants for P43815
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P43815 | |||||
No associated diseases with P43815
4 regional properties for P43815
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.7 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| alanine-tRNA ligase activity | Catalysis of the reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). |
| amino acid binding | Binding to an amino acid, organic acids containing one or more amino substituents. |
| aminoacyl-tRNA editing activity | The hydrolysis of an incorrectly aminoacylated tRNA. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| tRNA binding | Binding to a transfer RNA. |
| zinc ion binding | Binding to a zinc ion (Zn). |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| alanyl-tRNA aminoacylation | The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine accetping tRNA. |
| negative regulation of DNA-templated transcription | Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription. |
| tRNA modification | The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKTTAEIRQS | FLDFFHSKGH | QVVESSSLVP | ENDPTLLFTN | AGMNQFKDVF | LGMDKRPYSR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ATTAQRCVRP | GGKHNDLENV | GYTARHHTFF | EMLGNFSFGD | YFKQDAINFA | WEYLTSPQWL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GLPKEKLWVT | VYETDDEAYN | IWNKDVGVPA | ERIIRIGDNK | GSPYASDNFW | AMGDTGPCGP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CTEIFYDHGD | HIWGGPPGSP | EEDGDRYIEI | WNVVFMQFNR | LADGTMEKLP | RPSVDTGMGL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ERISAVLQHV | NSNYEIDIFK | TLIAKTAEIV | GATDLTNKSL | RVIADHIRSC | AYLIADGVIP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SNEGRGYVLR | RIIRRAVRHG | HLLGAKESFF | YKLVPTLIDV | MAEAGKDVKA | KQTNVEKLLR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LEEEQFARTL | ERGLSLLDEA | LSQVKDGILS | GEVAFKLYDT | YGFPLDLTAD | VCRERNITID |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EQAFDRKMEA | QRTRAQAASQ | FGVDYNSVIR | VDGETKFEGY | TEVESQAKIT | ALFYDGKSVE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SIEAGQSAVV | ILENTPFYAE | SGGQIGDSGY | LSTQSVTFNV | KDTQKYGQVF | GHIGELTQGS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LKVGQSVNAI | VDAKRRHNTS | LNHSATHLLH | AALRQILGLH | VVQKGSLVSD | KALRFDFAQP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EAITKEQLSE | IETLVNQKIR | ANFPVQTDIM | DIDSAKAKGA | MALFGEKYGD | KVRVLTMGDF |
| 670 | 680 | 690 | 700 | 710 | 720 |
| SIELCGGIHA | KRTGDIGLFK | IITENAVAAG | IRRIEAVTGQ | NAIDWLHNQQ | RILTQSADLL |
| 730 | 740 | 750 | 760 | 770 | 780 |
| KSDVNTLAEK | IQQLQDKAKK | VEKELQGLKE | KAAMQAGSYF | VKSAVKINGV | SVIAQQLDGI |
| 790 | 800 | 810 | 820 | 830 | 840 |
| ETKSLRVMVD | DLKNQLGSGV | IAFASILDEK | VNLVVGVTND | LTAKIKAGEL | VNLMAQQVGG |
| 850 | 860 | 870 | |||
| KGGGRPDMAM | AGGSQLENVT | QAIKVAQDWL | NKNL |